ID W6Q4V6_PENRF Unreviewed; 537 AA.
AC W6Q4V6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=D-aminopeptidase {ECO:0000313|EMBL:CDM31688.1};
GN Name=dap {ECO:0000313|EMBL:CDM31688.1};
GN ORFNames=PROQFM164_S02g001839 {ECO:0000313|EMBL:CDM31688.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM31688.1};
RN [1] {ECO:0000313|EMBL:CDM31688.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM31688.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the peptidase S12 family.
CC {ECO:0000256|ARBA:ARBA00038215}.
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DR EMBL; HG792016; CDM31688.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q4V6; -.
DR OMA; QFVCALL; -.
DR OrthoDB; 1931461at2759; -.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.50; -; 2.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR027279; D_amino_pept/lipop_sf.
DR InterPro; IPR012856; DAP_B_dom.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF07930; DAP_B; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF50886; D-aminopeptidase, middle and C-terminal domains; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:CDM31688.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:CDM31688.1};
KW Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:CDM31688.1}.
FT DOMAIN 17..330
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT DOMAIN 353..533
FT /note="D-aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF07930"
SQ SEQUENCE 537 AA; 59091 MW; E662AFB7903ACA0D CRC64;
MAIDEKVQAV LNKTVLRYRG PGGAIAVVKD GEVIGQRVWG FADLDQRIPM TAQTQIPICS
ITKQFVCALL IDLERNPTPT LAAKGDVRKQ LSDHLAEILS PELTSDGELT IDRLCDMQSG
MRDYWAMTTL WGSKPDDEFL IARDCGPLLA RTKSFMFQPG TEYSYCNVNF HVLARIIERA
TGESLAKLLE KRILRPAGMS TAFLCPNTAH HPPPCVGYEG DEQHGFTAAV NRMEWSGDAG
LVASLADMIE YEKYLDRCYA DPQSWYHTAI AAPKFKDGTP AKYRYGLDHA DIAGVNTIGH
GGALRGYRLH RRHAPRERLS VVVMSNSDFG AFGPNMEILH ELLGIPKPVA STVQPAADWV
GAFLDQDTQL SIVITKGARD GEVAIRYDGS AEPIKLSAPN HGKSDSMVAT IDGDFLSIHR
VVDNRILSAR RIVPKESILK GTSFQGVYHC AEIESTFHCI GEDGMLYGAF DGYLGQGIAT
PMKYLGDDVW VLTCPRGLDA PAPGDWTVVF SRDEHDAIQG FTIGCWLARK VDYVKRA
//
